We have observed that polyphosphate metabolites such as 2,3 DPG will dissociate the erythrocyte membrane skeleton or shell. This dissociation process does not involve 2,3 DPG hydrolysis of spectrin phosphates. Rather we believe dissociation occurs as the result of 2,3 DPG binding to and causing a conformation change in shell proteins. In the next year we plan to characterize the binding of 2,3 DPG to purified shell proteins, spectrin actin and band 4.1. Shells will be covalently modified to dettermine if the effect of 2,3 DPG can be blocked. Also, we will measure the effects of polyphosphates on gels of filamin and actin. These studies have particular relevance to our understanding of the control of cytoskeletal organization because it has not previously been suggested that polyphosphates can directly alter cytoskeletal assembly.